Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.
about
Activation of dioxygen by copper metalloproteins and insights from model complexes.Critical Aspects of Heme-Peroxo-Cu Complex Structure and Nature of Proton Source Dictate Metal-O(peroxo) Breakage versus Reductive O-O Cleavage Chemistry.Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase.Bioinspired Synthesis of Cu2+ -Modified Covalent Triazine Framework: A New Highly Efficient and Promising Peroxidase Mimic.Copper(I)/NO(g) Reductive Coupling Producing a trans-Hyponitrite Bridged Dicopper(II) Complex: Redox Reversal Giving Copper(I)/NO(g) Disproportionation.
P2860
Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Using Biosynthetic Models of H ...... ible for Enzymatic Activities.
@en
type
label
Using Biosynthetic Models of H ...... ible for Enzymatic Activities.
@en
prefLabel
Using Biosynthetic Models of H ...... ible for Enzymatic Activities.
@en
P2860
P356
P1476
Using Biosynthetic Models of H ...... ible for Enzymatic Activities.
@en
P2093
Ambika Bhagi-Damodaran
Igor Petrik
P2860
P304
P356
10.1002/IJCH.201600033
P50
P577
2016-09-16T00:00:00Z